IF5Z_ARATH
ID IF5Z_ARATH Reviewed; 437 AA.
AC Q9S825;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable eukaryotic translation initiation factor 5-2;
DE Short=eIF-5 2;
GN OrderedLocusNames=At1g77840; ORFNames=F28K19.5, T32E8.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP PHOSPHORYLATION AT SER-201; THR-230; SER-428; SER-431 AND SER-433.
RX PubMed=19509420; DOI=10.1074/jbc.m109.007658;
RA Dennis M.D., Person M.D., Browning K.S.;
RT "Phosphorylation of plant translation initiation factors by CK2 enhances
RT the in vitro interaction of multifactor complex components.";
RL J. Biol. Chem. 284:20615-20628(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC subunit results in the formation of a functional 80S initiation complex
CC (80S.mRNA.Met-tRNA[F]) (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-201, Thr-230, Ser-428, Ser-431, and Ser-433
CC by CK2. {ECO:0000269|PubMed:19509420}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; AC009243; AAF17676.1; -; Genomic_DNA.
DR EMBL; AC012193; AAG51628.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36033.1; -; Genomic_DNA.
DR EMBL; AY062694; AAL32772.1; -; mRNA.
DR EMBL; AY065097; AAL38273.1; -; mRNA.
DR EMBL; AY114664; AAM47983.1; -; mRNA.
DR EMBL; BT002163; AAN72174.1; -; mRNA.
DR RefSeq; NP_177907.1; NM_106433.4.
DR AlphaFoldDB; Q9S825; -.
DR SMR; Q9S825; -.
DR STRING; 3702.AT1G77840.1; -.
DR iPTMnet; Q9S825; -.
DR PaxDb; Q9S825; -.
DR PRIDE; Q9S825; -.
DR ProteomicsDB; 232278; -.
DR DNASU; 844119; -.
DR EnsemblPlants; AT1G77840.1; AT1G77840.1; AT1G77840.
DR GeneID; 844119; -.
DR Gramene; AT1G77840.1; AT1G77840.1; AT1G77840.
DR KEGG; ath:AT1G77840; -.
DR Araport; AT1G77840; -.
DR TAIR; locus:2029416; AT1G77840.
DR eggNOG; KOG2767; Eukaryota.
DR HOGENOM; CLU_026663_1_1_1; -.
DR InParanoid; Q9S825; -.
DR OMA; HSNGNEG; -.
DR OrthoDB; 979826at2759; -.
DR PhylomeDB; Q9S825; -.
DR PRO; PR:Q9S825; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S825; baseline and differential.
DR Genevisible; Q9S825; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..437
FT /note="Probable eukaryotic translation initiation factor 5-
FT 2"
FT /id="PRO_0000212523"
FT DOMAIN 278..436
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 148..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 201
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:19509420"
FT MOD_RES 230
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:19509420"
FT MOD_RES 428
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:19509420"
FT MOD_RES 431
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:19509420"
FT MOD_RES 433
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:19509420"
SQ SEQUENCE 437 AA; 48640 MW; 11855645569D15F2 CRC64;
MALQNIGASN RNDAFYRYKM PKMVTKTEGK GNGIKTNIIN NVEIAKALAR PPSYTTKYFG
CELGAQSKFD EKTGTSLVNG AHNTSKLAGL LENFIKKFVQ CYGCGNPETE IIITKTQMVN
LKCAACGFIS EVDMRDKLTN FILKNPPEQK KVSKDKKAMR KAEKERLKEG ELADEEQRKL
KAKKKALSNG KDSKTSKNHS SDEDISPKHD ENALEVDEDE DDDDGVEWQT DTSREAAEKR
MMEQLSAKTA EMVMLSAMEV EEKKAPKSKS NGNVVKTENP PPQEKNLVQD MKEYLKKGSP
ISALKSFISS LSEPPQDIMD ALFNALFDGV GKGFAKEVTK KKNYLAAAAT MQEDGSQMHL
LNSIGTFCGK NGNEEALKEV ALVLKALYDQ DIIEEEVVLD WYEKGLTGAD KSSPVWKNVK
PFVEWLQSAE SESEEED
